ID A0A0R1XKJ1_9LACO Unreviewed; 1051 AA.
AC A0A0R1XKJ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=PyrAB protein {ECO:0000313|EMBL:KRM28329.1};
GN ORFNames=FC91_GL001792 {ECO:0000313|EMBL:KRM28329.1};
OS Schleiferilactobacillus harbinensis DSM 16991.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM28329.1, ECO:0000313|Proteomes:UP000050949};
RN [1] {ECO:0000313|EMBL:KRM28329.1, ECO:0000313|Proteomes:UP000050949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM28329.1,
RC ECO:0000313|Proteomes:UP000050949};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM28329.1}.
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DR EMBL; AZFW01000032; KRM28329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1XKJ1; -.
DR PATRIC; fig|1122147.4.peg.1860; -.
DR eggNOG; COG0458; Bacteria.
DR Proteomes; UP000050949; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000050949};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 122..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 634..841
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 910..1051
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1051 AA; 114681 MW; 1DCCB708F0A86E05 CRC64;
MLGSGPNVLG QGAEFDKAGA AALGALHDAG YETIVINSNP ATVMTDTHSA DRVYVEPVTR
QFVSQIIRQE MPDAILATFG GQTALNLVME LANDGLLSEL HIKMLGTPLN AIEQTEDREL
FYNLLRNLQE PVPQATVVED PQDAVQFVQR VGWPVIVRPA YTLGGTGGGI AHSDKALAAF
VQNGITLSPT GQVAVERSID GYREIEIELV RDHADNTAVV AVLENIDPVG IHTGDSIVVT
PAQTLSHTEL TRLREAAIKI IRALEIEGVC DVQFAVDPNS DAYYVIEVNP RLGRSAVLAE
TATGYPVARV TAMLAIGQSL ADIPLSPAGA TAPTTAASEP VLDYLVTKLP RWSYQSVGAD
RRIGTQMKAS GEVVAFGRSL EESILKAMRS LTWDTDDEYL NRVRHFDDDT LASHLIHPED
DRLFAMLEAM QRGYSVSEVA ELTKIHPYFL ERLHHIVAML KTVADQAGDT DTLMAAKRLG
LSDRRIGELW QLPAEQVRAL RLEAKIVPHY SVSGTNDGNN FGPAKLFFST YGEAGQQTPM
QKDAVLVIGS GAYQTRQGQE FDYGTVHALN AIHRSGYAAI LVNCNAQAVS TDRDHSDRLY
FEPLTIEDIL NVVDAEKPVG VLTQFGGSTA ARFQTALSQA GVKLFDSPLT ELPKQSLKEP
LKLRGRIPTD PAHVTAQAAQ IGYPLWVSPS KRHFAAHAHF ITSAEMLAQF LTSAHLADDQ
VIRLQPYTDG ATYEVFGLKD DTDAYVAGIV EHLWAQNANV DHMLSVFPTN HLSAAQRTAL
AQVATTDLGQ MNARGVVQLT YIWQRDHFRR LYVQTIGGGS LPFFAKASGI PLVELATRIF
LGNTLKELPL PEITQKKRQT VYVWAPVFSV AKLTQQADDL NVTTYHTGEV MGKAGTFAKA
YYKTLAAGNN PFPNHGNILF TVADSDKSQA LKLARRFRAI GYQIQATPHT ANYFQAHHLP
IQRIQNKHAV ALSMAPQHNA DGPQAIVYTN DPMDAASIRD TVLIRNVTLV QGIPLFTELD
TLGALLNVLE SQRFATVPQG AEPEADDEDD E
//
